Activation and stabilization of intracellular aspartic proteinases by ATP.
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概要
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Cathepsin D and cathepsin E are two major intracellular aspartic proteinases in animal cells. Despite their similarity in catalytic properties, they have different structural and immunological properties. In order to investigate the mechanism which is responsible for the regulation of cathepsins D and E activities in cells, both enzymes were purified from different sources and the effects of ATP and its analogues on these enzymes' activities were determined. The hydrolyzing activity against bovine serum albumin at pH 4.5 by cathepsin D, which was purified from bovine and rat spleen, was markedly enhanced by nucleotides such as ATP, GTP and CTP. The non-hydrolyzable methylene-ATP analogue also showed an activation of this enzyme equivalent to that obtained with these nucleotides. However, this activation was not observed with bovine hemoglobin which is a preferential substrate for cathepsin D as well as cathepsin E. In contrast, the hemoglobin-hydrolyzing activity by cathepsin E, which was isolated from human erythrocytes and rat spleen, was also apparently activated by these compounds under the same conditions, whereas the albuminhydrolyzing activity was not affected by them. The activation potency of cathepsin E by ATP was found to be closely correlated to the thermostabilizing effect of ATP on this enzyme. These results indicate that the activation of these enzymes by these compounds is dependent on the substrates used and independent of energy. It is thus considered that these compounds may play important roles in regulating these enzymes in cells.
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